G
Gloria Fernández-Lorente
Researcher at Spanish National Research Council
Publications - 152
Citations - 11445
Gloria Fernández-Lorente is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Lipase & Immobilized enzyme. The author has an hindex of 47, co-authored 149 publications receiving 10412 citations. Previous affiliations of Gloria Fernández-Lorente include Autonomous University of Madrid.
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Improvement of enzyme activity, stability and selectivity via immobilization techniques
Cesar Mateo,Jose M. Palomo,Gloria Fernández-Lorente,Jose M. Guisan,Roberto Fernandez-Lafuente +4 more
TL;DR: In all cases, enzyme engineering via immobilization techniques is perfectly compatible with other chemical or biological approaches to improve enzyme functions and the final success depend on the availability of a wide battery of immobilization protocols.
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Immobilization of lipases by selective adsorption on hydrophobic supports.
Roberto Fernandez-Lafuente,Pilar Armisén,Pilar Sabuquillo,Gloria Fernández-Lorente,Jose M. Guisan +4 more
TL;DR: Different approaches for lipase immobilization mainly related to the further use of immobilized derivatives to carry out enantio and regioselective hydrolysis in high water-activity systems are reviewed.
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Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases
Jose M. Palomo,Gloria Muñoz,Gloria Fernández-Lorente,Cesar Mateo,Roberto Fernandez-Lafuente,Jose M. Guisan +5 more
TL;DR: It seems that the “open structure” of lipases, adsorbed on hydrophobic supports, is much more active and much more stable than the corresponding “closed” structure even when the closed structure is undergoing a very intense multipoint covalent attachment.
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Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins
Cesar Mateo,Jose M. Palomo,Manuel Fuentes,Lorena Betancor,Valeria Grazú,Fernando López-Gallego,Benevides C. C. Pessela,Aurelio Hidalgo,Gloria Fernández-Lorente,Roberto Fernandez-Lafuente,Jose M. Guisan +10 more
TL;DR: Very active and highly stabilized derivatives of many enzymes and proteins have been prepared using activated supports that immobilize proteins, via a two-point reaction involving the region/s of the protein surface with the higher densities of amino groups.
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Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage.
TL;DR: Multifunctional supports containing epoxy groups are proposed as a second generation of activated supports for covalent immobilization of enzymes following the epoxy chemistry on any type of support (hydrophobic or hydrophilic ones) under very mild experimental conditions.